Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterparts.

DNA repair - 4 Feb 2010

Guo Yin, Bandaru Viswanath, Jaruga Pawel, Zhao Xiaobei, Burrows Cynthia J, Iwai Shigenori, Dizdaroglu Miral, Bond Jeffrey P, Wallace Susan S

Abstract excerpt

The DNA glycosylases that remove oxidized DNA bases fall into two general families: the Fpg/Nei family and the Nth superfamily. Based on protein sequence alignments, we identified four putative Fpg/Nei family members, as well as a putative Nth protein in Mycobacterium tuberculosis H37Rv. All four Fpg/Nei proteins were successfully overexpressed using a bicistronic vector created in our laboratory. The MtuNth...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to DNA Glycosylases
Share to DNA, Single-Stranded

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gas Chromatography-Mass Spectrometry

Share to Pseudogenes

Share to Purines

Share to Pyrimidines

Share to Rifampin

Share to Stereoisomerism

Source

Open in PubMed Open full text

Identifiers

PMID: 20031487
DOI: 10.1016/j.dnarep.2009.11.008
PMCID: PMC2836239

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterparts.PMID 20031487Read ↗

Substrate specificities and functional characterization of a thermo-tolerant uracil DNA glycosylase (UdgB) from Mycobacterium tuberculosis.Semantic proximity Read ↗

The contribution of Nth and Nei DNA glycosylases to mutagenesis in Mycobacterium smegmatis.Semantic proximity Read ↗

A combinatorial role for MutY and Fpg DNA glycosylases in mutation avoidance in Mycobacterium smegmatis.Semantic proximity Read ↗

Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA.Semantic proximity Read ↗

A multilayered repair system protects the mycobacterial chromosome from endogenous and antibiotic-induced oxidative damage.Semantic proximity Read ↗

A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-regulation of accumulation of G, C mutations and protection against oxidative stress in mycobacteria.Semantic proximity Read ↗

Mycobacterium tuberculosis MutT1 (Rv2985) and ADPRase (Rv1700) proteins constitute a two-stage mechanism of 8-oxo-dGTP and 8-oxo-GTP detoxification and adenosine to cytidine mutation avoidance.Semantic proximity Read ↗

The mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and in vivo.Semantic proximity Read ↗

Synergistic effects of UdgB and Ung in mutation prevention and protection against commonly encountered DNA damaging agents in Mycobacterium smegmatis.Semantic proximity Read ↗

Human NEIL3 is mainly a monofunctional DNA glycosylase removing spiroimindiohydantoin and guanidinohydantoin.Semantic proximity Read ↗

DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells.Semantic proximity Read ↗

Uracil DNA glycosylase (UDG) activities in Bradyrhizobium diazoefficiens: characterization of a new class of UDG with broad substrate specificity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.